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Protein

Vacuolar-sorting protein SNF7

Gene

SNF7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts a component of the ESCRT-III complex required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB) (PubMed:11559748, PubMed:12194857). The sequential action of ESCRT-0, -I, and -II together with the ordered assembly of ESCRT-III links membrane invagination to cargo sorting (PubMed:12194857). Membrane scission in the neck of the growing vesicle releases mature, cargo-laden ILVs into the lumen (PubMed:24139821, PubMed:24711499). ESCRT-III is critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery (PubMed:24139821, PubMed:24711499). SNF7 is the most abundant ESCRT-III subunit which forms membrane-sculpting filaments with 30 Angstrom periodicity and a exposed cationic membrane-binding surface (PubMed:26670543). Its activation requires a prominent conformational rearrangement to expose protein-membrane and protein-protein interfaces (PubMed:26670543). SNF7 filaments then form spirals that could function as spiral springs (PubMed:26522593). The elastic expansion of compressed SNF7 spirals generates an area difference between the two sides of the membrane and thus curvature which could be the origin of membrane deformation leading eventually to fission (PubMed:26522593). SNF7 recruits BRO1, which in turn recruits DOA4, which deubiquitinates cargos before their enclosure within MVB vesicles (PubMed:11029042, PubMed:15935782). ESCRT-III is also recruited to the nuclear envelope (NE) by integral INM proteins to surveil and clear defective nuclear pore complex (NPC) assembly intermediates to ensure the fidelity of NPC assembly (PubMed:25303532).8 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

  • cellular response to anoxia Source: SGD
  • intralumenal vesicle formation Source: SGD
  • late endosome to vacuole transport Source: SGD
  • protein transport Source: UniProtKB-KW
  • ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-32186-MONOMER.
ReactomeiR-SCE-1632852. Macroautophagy.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar-sorting protein SNF7Curated
Alternative name(s):
DOA4-independent degradation protein 11 Publication
Sucrose nonfermenting protein 71 Publication
Vacuolar protein-sorting-associated protein 321 Publication
Gene namesi
Name:SNF71 Publication
Synonyms:DID11 Publication, VPS321 Publication
Ordered Locus Names:YLR025WImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR025W.
SGDiS000004015. SNF7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • ESCRT III complex Source: SGD
  • nuclear envelope Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Exhibits defects in the sorting and processing of native vacuolar proteins (PubMed:3062374).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 21W → E: Impairs binding to membrane. 1 Publication
Mutagenesisi6 – 61F → E: Impairs binding to membrane. 1 Publication
Mutagenesisi8 – 81W → E: Impairs binding to membrane. 1 Publication
Mutagenesisi25 – 251R → E: Leads to severe sorting defects; when associated with E-29 and E-36. 1 Publication
Mutagenesisi29 – 291H → E: Leads to severe sorting defects; when associated with E-25 and E-36. 1 Publication
Mutagenesisi36 – 361K → E: Leads to severe sorting defects; when associated with E-25 and E-29. 1 Publication
Mutagenesisi52 – 521R → E: Impairs the formation of protofilaments; when associated with K-90. Also impairs the formation of protofilaments; when associated with E-94. Also impairs the formation of protofilaments; when associated with E-107. Also impairs the formation of protofilaments; when associated with E-114. 1 Publication
Mutagenesisi83 – 831T → E: Leads to severe sorting defects. 1 Publication
Mutagenesisi87 – 871M → E: Leads to severe sorting defects. 1 Publication
Mutagenesisi90 – 901Q → K: Leads to severe sorting defects. Impairs the formation of protofilaments; when associated with E-52. 1 Publication
Mutagenesisi94 – 941I → E: Leads to severe sorting defects. Impairs the formation of protofilaments; when associated with E-52. 1 Publication
Mutagenesisi95 – 951E → K: Leads to severe sorting defects; when associated with K-102 and K-109. 1 Publication
Mutagenesisi97 – 971A → K: Leads to severe sorting defects. 1 Publication
Mutagenesisi99 – 991L → K: Leads to severe sorting defects. 1 Publication
Mutagenesisi101 – 1011L → E: Leads to severe sorting defects. 1 Publication
Mutagenesisi102 – 1021E → K: Leads to severe sorting defects; when associated with K-95 and K-109. 1 Publication
Mutagenesisi103 – 1031T → E: Leads to severe sorting defects. 1 Publication
Mutagenesisi104 – 1041M → E: Leads to severe sorting defects. 1 Publication
Mutagenesisi107 – 1071M → E: Leads to severe sorting defects. Impairs the formation of protofilaments; when associated with E-52. 1 Publication
Mutagenesisi109 – 1091E → K: Leads to severe sorting defects; when associated with K-95 and K-102. 1 Publication
Mutagenesisi114 – 1141M → E: Leads to severe sorting defects. Impairs the formation of protofilaments; when associated with E-52. 1 Publication
Mutagenesisi117 – 1171I → E: Leads to severe sorting defects. 1 Publication
Mutagenesisi121 – 1211L → D: Leads to severe sorting defects. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 240240Vacuolar-sorting protein SNF7PRO_0000211446Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721PhosphothreonineCombined sources
Modified residuei119 – 1191PhosphoserineCombined sources
Modified residuei193 – 1931PhosphoserineCombined sources
Cross-linki229 – 229Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP39929.

PTM databases

iPTMnetiP39929.

Interactioni

Subunit structurei

Core component of the ESCRT-III complex (endosomal sorting required for transport complex III) (PubMed:12194857, PubMed:18854142). ESCRT-III appears to be sequentially assembled as a flat lattice on the endosome membrane and forms a transient 450 kDa complex that contains DID4, oligomerized SNF7, VPS20 and VPS24 (PubMed:18854142). SNF7 polymerizes into spirals at the surface of lipid bilayers (PubMed:26522593). SNF7 polymerization is nucleated by association of SNF7 with VPS20; the process is terminated through association of VPS24, possibly by capping the SNF7 filament (PubMed:24058170, PubMed:24711499). Interacts with VTA1; the interaction requires DID2 (PubMed:16601096, PubMed:24058170). Interacts with BRO1 (PubMed:15086794, PubMed:15935782, PubMed:24058170). Interacts with DOA4 (PubMed:26427873). Interacts with HEH1 and HEH2 (PubMed:25303532). Interacts with RIM20 and YGR122W (PubMed:24058170).10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-17554,EBI-17554
BRO1P485823EBI-17554,EBI-3768
DID4P361084EBI-17554,EBI-26574
HEH2Q032813EBI-17554,EBI-22131
VPS20Q042724EBI-17554,EBI-28157
VPS4P529174EBI-17554,EBI-20475

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi31299. 129 interactions.
DIPiDIP-1747N.
IntActiP39929. 28 interactions.
MINTiMINT-389266.

Structurei

Secondary structure

1
240
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 5638Combined sources
Helixi60 – 11859Combined sources
Turni120 – 1223Combined sources
Helixi127 – 13812Combined sources
Turni139 – 1413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5FD7X-ray2.40A12-150[»]
5FD9X-ray1.60A12-150[»]
ProteinModelPortaliP39929.
SMRiP39929. Positions 20-95, 121-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi68 – 714Poly-Lys
Compositional biasi216 – 22813Asp/Glu-rich (acidic)Add
BLAST

Domaini

The N-terminus (residues 1 to 11) forms an amphipatic helix which is required for the association to membrane.1 Publication

Sequence similaritiesi

Belongs to the SNF7 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000005006.
HOGENOMiHOG000209960.
InParanoidiP39929.
KOiK12194.
OMAiLESANMN.
OrthoDBiEOG092C50TH.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39929-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWSSLFGWTS SNAKNKESPT KAIVRLREHI NLLSKKQSHL RTQITNQENE
60 70 80 90 100
ARIFLTKGNK VMAKNALKKK KTIEQLLSKV EGTMESMEQQ LFSIESANLN
110 120 130 140 150
LETMRAMQEG AKAMKTIHSG LDIDKVDETM DEIREQVELG DEISDAISRP
160 170 180 190 200
LITGANEVDE DELDEELDML AQENANQETS KIVNNNVNAA PISENKVSLP
210 220 230 240
SVPSNKIKQS ENSVKDGEEE EDEEDEDEKA LRELQAEMGL
Length:240
Mass (Da):26,987
Last modified:February 1, 1995 - v1
Checksum:i5241A18BB181F0C1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731E → G in AAS56528 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09751 Genomic DNA. No translation available.
Z73197 Genomic DNA. Translation: CAA97548.1.
AY558202 Genomic DNA. Translation: AAS56528.1.
BK006945 Genomic DNA. Translation: DAA09343.1.
PIRiS52590.
RefSeqiNP_013125.1. NM_001181912.1.

Genome annotation databases

EnsemblFungiiYLR025W; YLR025W; YLR025W.
GeneIDi850712.
KEGGisce:YLR025W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09751 Genomic DNA. No translation available.
Z73197 Genomic DNA. Translation: CAA97548.1.
AY558202 Genomic DNA. Translation: AAS56528.1.
BK006945 Genomic DNA. Translation: DAA09343.1.
PIRiS52590.
RefSeqiNP_013125.1. NM_001181912.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5FD7X-ray2.40A12-150[»]
5FD9X-ray1.60A12-150[»]
ProteinModelPortaliP39929.
SMRiP39929. Positions 20-95, 121-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31299. 129 interactions.
DIPiDIP-1747N.
IntActiP39929. 28 interactions.
MINTiMINT-389266.

PTM databases

iPTMnetiP39929.

Proteomic databases

MaxQBiP39929.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR025W; YLR025W; YLR025W.
GeneIDi850712.
KEGGisce:YLR025W.

Organism-specific databases

EuPathDBiFungiDB:YLR025W.
SGDiS000004015. SNF7.

Phylogenomic databases

GeneTreeiENSGT00390000005006.
HOGENOMiHOG000209960.
InParanoidiP39929.
KOiK12194.
OMAiLESANMN.
OrthoDBiEOG092C50TH.

Enzyme and pathway databases

BioCyciYEAST:G3O-32186-MONOMER.
ReactomeiR-SCE-1632852. Macroautophagy.

Miscellaneous databases

PROiP39929.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSNF7_YEAST
AccessioniPrimary (citable) accession number: P39929
Secondary accession number(s): D6VY27, E9P8V6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 7, 2016
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 3270 molecules/cell in log phase SD medium.1 Publication

Caution

Was originally thought to be a nuclear protein and mutations were shown to prevent full derepression of the SUC2 (invertase) gene.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.